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==Crystal structure of D-mannonate dehydratase homolog from Chromohalobacter salexigens (Target EFI-502114), with bound NA, ordered loop==
==Crystal structure of D-mannonate dehydratase homolog from Chromohalobacter salexigens (Target EFI-502114), with bound NA, ordered loop==
<StructureSection load='4f4r' size='340' side='right' caption='[[4f4r]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='4f4r' size='340' side='right'caption='[[4f4r]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4f4r]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chrsd Chrsd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F4R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F4R FirstGlance]. <br>
<table><tr><td colspan='2'>[[4f4r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chromohalobacter_salexigens_DSM_3043 Chromohalobacter salexigens DSM 3043]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F4R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F4R FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Csal_2974 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=290398 CHRSD])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mannonate_dehydratase Mannonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.8 4.2.1.8] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4f4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f4r OCA], [https://pdbe.org/4f4r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f4r RCSB], [https://www.ebi.ac.uk/pdbsum/4f4r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f4r ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4f4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f4r OCA], [http://pdbe.org/4f4r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4f4r RCSB], [http://www.ebi.ac.uk/pdbsum/4f4r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4f4r ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DMGD_CHRSD DMGD_CHRSD] Has low dehydratase activity with D-mannonate and D-gluconate, suggesting that these are not physiological substrates and that it has no significant role in the in vivo degradation of these compounds. Has no detectable activity with a panel of 70 other acid sugars (in vitro).<ref>PMID:24697546</ref>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Chrsd]]
[[Category: Chromohalobacter salexigens DSM 3043]]
[[Category: Mannonate dehydratase]]
[[Category: Large Structures]]
[[Category: Almo, S C]]
[[Category: Al Obaidi NF]]
[[Category: Bhosle, R]]
[[Category: Almo SC]]
[[Category: Chowdhury, S]]
[[Category: Bhosle R]]
[[Category: EFI, Enzyme Function Initiative]]
[[Category: Chowdhury S]]
[[Category: Evans, B]]
[[Category: Evans B]]
[[Category: Gerlt, J A]]
[[Category: Gerlt JA]]
[[Category: Glenn, A Scott]]
[[Category: Hammonds J]]
[[Category: Hammonds, J]]
[[Category: Hillerich B]]
[[Category: Hillerich, B]]
[[Category: Imker HJ]]
[[Category: Imker, H J]]
[[Category: Love J]]
[[Category: Love, J]]
[[Category: Morisco LL]]
[[Category: Morisco, L L]]
[[Category: Scott Glenn A]]
[[Category: Obaidi, N F.Al]]
[[Category: Seidel RD]]
[[Category: Seidel, R D]]
[[Category: Sojitra S]]
[[Category: Sojitra, S]]
[[Category: Toro R]]
[[Category: Toro, R]]
[[Category: Vetting MW]]
[[Category: Vetting, M W]]
[[Category: Washington E]]
[[Category: Washington, E]]
[[Category: Wasserman SR]]
[[Category: Wasserman, S R]]
[[Category: Enolase]]
[[Category: Enzyme function initiative]]
[[Category: Lyase]]
[[Category: Structural genomic]]

Latest revision as of 18:16, 14 March 2024

Crystal structure of D-mannonate dehydratase homolog from Chromohalobacter salexigens (Target EFI-502114), with bound NA, ordered loopCrystal structure of D-mannonate dehydratase homolog from Chromohalobacter salexigens (Target EFI-502114), with bound NA, ordered loop

Structural highlights

4f4r is a 1 chain structure with sequence from Chromohalobacter salexigens DSM 3043. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DMGD_CHRSD Has low dehydratase activity with D-mannonate and D-gluconate, suggesting that these are not physiological substrates and that it has no significant role in the in vivo degradation of these compounds. Has no detectable activity with a panel of 70 other acid sugars (in vitro).[1]

References

  1. ↑ Wichelecki DJ, Balthazor BM, Chau AC, Vetting MW, Fedorov AA, Fedorov EV, Lukk T, Patskovsky YV, Stead MB, Hillerich BS, Seidel RD, Almo SC, Gerlt JA. Discovery of function in the enolase superfamily: D-mannonate and d-gluconate dehydratases in the D-mannonate dehydratase subgroup. Biochemistry. 2014 Apr 29;53(16):2722-31. doi: 10.1021/bi500264p. Epub 2014 Apr, 15. PMID:24697546 doi:http://dx.doi.org/10.1021/bi500264p

4f4r, resolution 1.80Å

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